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17 Nov 2019
An enzyme catalyst mechanism that uses a metal cation to stabilize a negative charge in the active site is a: The catalytic mechanism that forces two substrates into an appropriate 3-dimensional arrangement so that the reaction can occur is: In conducting an experiment with a new drug, you find that regardless of the concentration of substrate, the drug is able to inhibit the enzyme activity at least a little bit. The inhibition is even more pronounced at low substrate concentrations. You are likely to not have w hat kind of inhibitor Draw what an uncompetitive inhibitor reaction will look like on a double-reciprocal plot. Include The non-inbuild reaction, too. Where on the enzyme will a suicide inhibitor bind?. What is the catalytic triad found in chymotrypsin? What conclusion can be drawn concerning an inhibitor if the KM is the same in the presence and absence of the inhibitor? The inhibitor binds to the substrate. The inhibitor has a structure that is not very similar to the substrate. The inhibitor forms a reversible covalent bond with the enzyme. The inhibitor binds to the same active site as the substrate, The Vmax is larger in the presence of inhibitor. What type(s) of inhibition can be reversed? competitive noncompetitive uncompetitive All of the above, None of the above.
An enzyme catalyst mechanism that uses a metal cation to stabilize a negative charge in the active site is a: The catalytic mechanism that forces two substrates into an appropriate 3-dimensional arrangement so that the reaction can occur is: In conducting an experiment with a new drug, you find that regardless of the concentration of substrate, the drug is able to inhibit the enzyme activity at least a little bit. The inhibition is even more pronounced at low substrate concentrations. You are likely to not have w hat kind of inhibitor Draw what an uncompetitive inhibitor reaction will look like on a double-reciprocal plot. Include The non-inbuild reaction, too. Where on the enzyme will a suicide inhibitor bind?. What is the catalytic triad found in chymotrypsin? What conclusion can be drawn concerning an inhibitor if the KM is the same in the presence and absence of the inhibitor? The inhibitor binds to the substrate. The inhibitor has a structure that is not very similar to the substrate. The inhibitor forms a reversible covalent bond with the enzyme. The inhibitor binds to the same active site as the substrate, The Vmax is larger in the presence of inhibitor. What type(s) of inhibition can be reversed? competitive noncompetitive uncompetitive All of the above, None of the above.
Deanna HettingerLv2
24 Sep 2019